A detailed investigation of the helical part of the resin-supported peptide catalyst possessing a turn motif and helical unit was conducted to clarify the structure-activity relationship. The peptide catalyst with an a-or 3 10 -helical tether was effective for an enantioselective Friedel-Crafts-type alkylation in water. From the spectral analysis of the peptide with an optimum sequence, it was demonstrated that the helical moiety of the peptide catalyst played a role for stabilizing a terminal turn structure.
A resin-supported N-terminal prolyl peptide having a beta-turn motif and hydrophobic polyleucine chain effectively catalyzed the asymmetric transfer hydrogenation under aqueous conditions. The polyleucine tether provides a hydrophobic cavity in aqueous media that brought about a remarkable acceleration of the reaction. In addition, the polyleucine chain also turned out to be essential for high enantioselectivity.
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